Therefore, the use of McLuc1 with different N-terminal luciferase fragments allows precise and quantitative detection of multiple protein interactions in living cells.
This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.
The formation of multiple protein interactions with DNA results in a decrease in protein-protein affinity and an increase in protein-DNA affinity with a net gain in overall stability for a protein-protein-DNA complex.
Clathrin is a three-legged molecule with a central hub domain from which three ∼190 kDa heavy chains are extended, each ending in an N-terminal seven-bladed β-propeller domain that allows for multiple protein interactions with various specificities between its blades [1].
WD40 domains can thus act as large interaction platforms for multiple protein interactions.
This result establishes that multicolour BiFC can be performed in the Drosophila embryo for simultaneous visualization of multiple protein interactions.
